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Apolipophorin-III Acts as a Positive Regulator of Plasmodium Development in Anopheles stephensi

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ABSTRACT

Apolipophorin III (ApoLp-III) is a well-known hemolymph protein having a functional role in lipid transport and immune responses of insects. Here we report the molecular and functional characterization of Anopheles stephensi Apolipophorin-III (AsApoLp-III) gene. This gene consists of 679 nucleotides arranged into two exons of 45 and 540 bp that give an ORF encoding 194 amino acid residues. Excluding a putative signal peptide of the first 19 amino acid residues, the 175-residues in mature AsApoLp-III protein has a calculated molecular mass of 22 kDa. Phylogenetic analysis revealed the divergence of mosquitoes (Order Diptera) ApoLp-III from their counterparts in moths (Order: Lepidoptera). Also, it revealed a close relatedness of AsApoLp-III to ApoLp-III of An. gambiae. AsApoLp-III mRNA expression is strongly induced in Plasmodium berghei infected mosquito midguts suggesting its crucial role in parasite development. AsApoLp-III silencing decreased P. berghei oocysts numbers by 7.7 fold against controls. These effects might be due to the interruption of AsApoLp-III mediated lipid delivery to the developing oocysts. In addition, nitric oxide synthase (NOS), an antiplasmodial gene, is also highly induced in AsApoLp-III silenced midguts suggesting that this gene acts like an agonist and protects Plasmodium against the mosquito immunity.

No MeSH data available.


Predicted 3D structure of putative AsApoLp-III protein. The AsApoLp-III protein consists of five long alpha-helices connected through short loops. The predicted model was constructed based on the M. sexta ApoLp-III as the template [PDB id: 1eq1]. Protein structures were predicted using Phyre2 server.
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Figure 3: Predicted 3D structure of putative AsApoLp-III protein. The AsApoLp-III protein consists of five long alpha-helices connected through short loops. The predicted model was constructed based on the M. sexta ApoLp-III as the template [PDB id: 1eq1]. Protein structures were predicted using Phyre2 server.

Mentions: Tertiary structure of the predicted AsApoLp-III protein was generated by Phyre2 program as before (Kelly and Sternberg, 2009). Of all, 89% of its total residues were modeled with 99.7% confidence against Manduca sexta ApoLp-III as reference (PDB ID: 1EQ1) (Figure 3). It is observed that despite the disparate similarity in the primary structure of ApoLp-III protein, ranging from >70% with dipterans to as low as 19% with lepidopteran, there seem to be a firm conservation in the tertiary structure of the protein (Gupta et al., 2010). These findings indicated that the functional conservation of this protein might have a minor selection pressure. The Ramchandran Plot analysis predicted that 98% residues of the proposed model of AsApoLp-III lie in favorable region rendering the reliability of this model.


Apolipophorin-III Acts as a Positive Regulator of Plasmodium Development in Anopheles stephensi
Predicted 3D structure of putative AsApoLp-III protein. The AsApoLp-III protein consists of five long alpha-helices connected through short loops. The predicted model was constructed based on the M. sexta ApoLp-III as the template [PDB id: 1eq1]. Protein structures were predicted using Phyre2 server.
© Copyright Policy
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC5383653&req=5

Figure 3: Predicted 3D structure of putative AsApoLp-III protein. The AsApoLp-III protein consists of five long alpha-helices connected through short loops. The predicted model was constructed based on the M. sexta ApoLp-III as the template [PDB id: 1eq1]. Protein structures were predicted using Phyre2 server.
Mentions: Tertiary structure of the predicted AsApoLp-III protein was generated by Phyre2 program as before (Kelly and Sternberg, 2009). Of all, 89% of its total residues were modeled with 99.7% confidence against Manduca sexta ApoLp-III as reference (PDB ID: 1EQ1) (Figure 3). It is observed that despite the disparate similarity in the primary structure of ApoLp-III protein, ranging from >70% with dipterans to as low as 19% with lepidopteran, there seem to be a firm conservation in the tertiary structure of the protein (Gupta et al., 2010). These findings indicated that the functional conservation of this protein might have a minor selection pressure. The Ramchandran Plot analysis predicted that 98% residues of the proposed model of AsApoLp-III lie in favorable region rendering the reliability of this model.

View Article: PubMed Central - PubMed

ABSTRACT

Apolipophorin III (ApoLp-III) is a well-known hemolymph protein having a functional role in lipid transport and immune responses of insects. Here we report the molecular and functional characterization of Anopheles stephensi Apolipophorin-III (AsApoLp-III) gene. This gene consists of 679 nucleotides arranged into two exons of 45 and 540 bp that give an ORF encoding 194 amino acid residues. Excluding a putative signal peptide of the first 19 amino acid residues, the 175-residues in mature AsApoLp-III protein has a calculated molecular mass of 22 kDa. Phylogenetic analysis revealed the divergence of mosquitoes (Order Diptera) ApoLp-III from their counterparts in moths (Order: Lepidoptera). Also, it revealed a close relatedness of AsApoLp-III to ApoLp-III of An. gambiae. AsApoLp-III mRNA expression is strongly induced in Plasmodium berghei infected mosquito midguts suggesting its crucial role in parasite development. AsApoLp-III silencing decreased P. berghei oocysts numbers by 7.7 fold against controls. These effects might be due to the interruption of AsApoLp-III mediated lipid delivery to the developing oocysts. In addition, nitric oxide synthase (NOS), an antiplasmodial gene, is also highly induced in AsApoLp-III silenced midguts suggesting that this gene acts like an agonist and protects Plasmodium against the mosquito immunity.

No MeSH data available.